Abstract
A new approach has been developed for quantification of the activity of endo-xylogluc an transferase, a novel enzyme that mediates the transfer of a segment of one xyloglucan molecule to another xyloglucan molecule. Purified xyloglucans with defined molecular-weight distributions and their fluorescent derivatives (pyridylamino xyloglucans) were used as substrates for the enzymatic reaction. The transferase activity was quantified by monitoring changes in molecularweight distributions of substrates by an alkali compatible gel permeation chromatographic system, equipped with a pulsed amperometric detector and a fluorescence detector. This new method was applied to the rapid detection and characterization of a novel transferase derived from plant tissues.
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